Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 536463
Title Bacteriophage DNA glucosylation impairs target DNA binding by type I and II but not by type V CRISPR–Cas effector complexes
Author(s) Vlot, Marnix; Houkes, Joep; Lochs, Silke J.A.; Swarts, Daan C.; Zheng, Peiyuan; Kunne, Tim; Mohanraju, Prarthana; Anders, Carolin; Jinek, Martin; Oost, John Van Der; Dickman, Mark J.; Brouns, Stan J.J.
Source Nucleic Acids Research 46 (2018)2. - ISSN 0305-1048 - p. 873 - 885.
DOI https://doi.org/10.1093/nar/gkx1264
Department(s) Microbiological Laboratory
Food Microbiology Laboratory
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2018
Abstract Prokaryotes encode various host defense systems that provide protection against mobile genetic elements. Restriction–modification (R–M) and CRISPR–Cas systems mediate host defense by sequence specific targeting of invasive DNA. T-even bacteriophages employ covalent modifications of nucleobases to avoid binding and therefore cleavage of their DNA by restriction endonucleases. Here, we describe that DNA glucosylation of bacteriophage genomes affects interference of some but not all CRISPR–Cas systems. We show that glucosyl modification of 5-hydroxymethylated cytosines in the DNA of bacteriophage T4 interferes with type I-E and type II-A CRISPR–Cas systems by lowering the affinity of the Cascade and Cas9–crRNA complexes for their target DNA. On the contrary, the type V-A nuclease Cas12a (also known as Cpf1) is not impaired in binding and cleavage of glucosylated target DNA, likely due to a more open structural architecture of the protein. Our results suggest that CRISPR–Cas systems have contributed to the selective pressure on phages to develop more generic solutions to escape sequence specific host defense systems.
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